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A Theory for Rate Constants in Rotation Trajectories of F_1-ATPase

Volkán-Kacsó, Sándor and Marcus, Rudolph (2018) A Theory for Rate Constants in Rotation Trajectories of F_1-ATPase. Biophysical Journal, 114 (3). 519a. ISSN 0006-3495.

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I present an elastic chemo-mechanical theory to treat single molecule imaging and “stalling” experiments in the F1-ATPase enzyme. Using a molecular group transfer approach the theory couples chemical reactions in the stator and the physics of torsional elasticity in the rotor. In the theory we predicted and compared with experiment the rate and equilibrium constant dependence of steps such as ATP binding as a function of the rotor angle.[PNAS, 112, 14230 (2015)] Using independent experimental data from biochemical ensemble and single-molecule imaging experiments, the model correctly predicts the controlled rotation data on fluorescent ATP without any adjustable parameters. We took into account the biasing effect of finite experimental time resolution in the single fluorescence trajectories and treated these data by developing computational statistical methods.[PNAS, 113 (48), 12029 (2016)] A theory-based method for the extraction of rate constants for hydrolysis and synthesis from controlled rotation data was also provided for angular range where no such data is currently available [PNAS, 114, 7272 (2016)] The framework is generic and we plan to apply it to other biomolecular motors.

Item Type:Article
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Marcus, Rudolph0000-0001-6547-1469
Additional Information:© 2018 Elsevier Inc. Available online 6 February 2018.
Issue or Number:3
Record Number:CaltechAUTHORS:20180510-132615402
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Official Citation:A Theory for Rate Constants in Rotation Trajectories of F1-ATPase Volkan-Kacso, Sandor et al. Biophysical Journal , Volume 114 , Issue 3 , 519a
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:86339
Deposited By: Tony Diaz
Deposited On:10 May 2018 20:46
Last Modified:22 Nov 2019 09:58

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